HEADER IMMUNE SYSTEM 04-FEB-16 5I0Q
TITLE STRUCTURE OF HUMAN C4B-BINDING PROTEIN ALPHA CHAIN CCP DOMAINS 1 AND 2
TITLE 2 IN COMPLEX WITH THE HYPERVARIABLE REGION OF MUTANT GROUP A
TITLE 3 STREPTOCOCCUS M2 (K65A, N66A) PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: M PROTEIN, SEROTYPE 2.1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 42-141;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: C4B-BINDING PROTEIN ALPHA CHAIN;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: UNP RESIDUES 49-172;
COMPND 10 SYNONYM: C4BP,PROLINE-RICH PROTEIN,PRP;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PYOGENES;
SOURCE 3 ORGANISM_TAXID: 1314;
SOURCE 4 GENE: EMML2.1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 GENE: C4BPA, C4BP;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS M PROTEIN, COMPLEMENT, STREPTOCOCCUS PYOGENES, HYPERVARIABLE ANTIGEN,
KEYWDS 2 IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR C.Z.BUFFALO,A.J.BAHN-SUH,P.GHOSH
REVDAT 2 26-OCT-16 5I0Q 1 JRNL
REVDAT 1 20-JUL-16 5I0Q 0
JRNL AUTH C.Z.BUFFALO,A.J.BAHN-SUH,S.P.HIRAKIS,T.BISWAS,R.E.AMARO,
JRNL AUTH 2 V.NIZET,P.GHOSH
JRNL TITL CONSERVED PATTERNS HIDDEN WITHIN GROUP A STREPTOCOCCUS M
JRNL TITL 2 PROTEIN HYPERVARIABILITY RECOGNIZE HUMAN C4B-BINDING
JRNL TITL 3 PROTEIN.
JRNL REF NAT MICROBIOL V. 1 16155 2016
JRNL REFN ESSN 2058-5276
JRNL PMID 27595425
JRNL DOI 10.1038/NMICROBIOL.2016.155
REMARK 2
REMARK 2 RESOLUTION. 2.29 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.29
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.53
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 47375
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.060
REMARK 3 FREE R VALUE TEST SET COUNT : 2568
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.5442 - 4.9396 1.00 4286 471 0.1997 0.2270
REMARK 3 2 4.9396 - 3.9212 1.00 4277 476 0.1696 0.1834
REMARK 3 3 3.9212 - 3.4257 1.00 4276 475 0.2005 0.2217
REMARK 3 4 3.4257 - 3.1126 1.00 4267 475 0.2059 0.2213
REMARK 3 5 3.1126 - 2.8895 1.00 4249 477 0.2125 0.2449
REMARK 3 6 2.8895 - 2.7191 1.00 4278 482 0.2173 0.2413
REMARK 3 7 2.7191 - 2.5830 1.00 4276 480 0.1984 0.2179
REMARK 3 8 2.5830 - 2.4705 1.00 4241 475 0.2177 0.2240
REMARK 3 9 2.4705 - 2.3754 1.00 4274 485 0.2533 0.2737
REMARK 3 10 2.3754 - 2.2935 0.98 4185 470 0.2593 0.2885
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.000
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 1283
REMARK 3 ANGLE : 1.416 1728
REMARK 3 CHIRALITY : 0.060 190
REMARK 3 PLANARITY : 0.005 224
REMARK 3 DIHEDRAL : 16.459 474
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 53 THROUGH 57 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.3716 46.5692 85.9653
REMARK 3 T TENSOR
REMARK 3 T11: 0.8806 T22: 1.0216
REMARK 3 T33: 0.7369 T12: 0.0986
REMARK 3 T13: 0.2326 T23: 0.4382
REMARK 3 L TENSOR
REMARK 3 L11: 7.7316 L22: 2.1555
REMARK 3 L33: 5.8220 L12: 0.2339
REMARK 3 L13: 1.3160 L23: 0.4313
REMARK 3 S TENSOR
REMARK 3 S11: -0.1585 S12: -0.8487 S13: -1.3668
REMARK 3 S21: 0.2979 S22: -0.1199 S23: 0.3268
REMARK 3 S31: 1.9439 S32: -0.8488 S33: 0.2938
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 58 THROUGH 86 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.2422 54.6855 63.9281
REMARK 3 T TENSOR
REMARK 3 T11: 0.5853 T22: 0.5888
REMARK 3 T33: 0.4409 T12: -0.2991
REMARK 3 T13: 0.0595 T23: 0.2146
REMARK 3 L TENSOR
REMARK 3 L11: 3.8089 L22: 4.2175
REMARK 3 L33: 5.3894 L12: 0.5913
REMARK 3 L13: 0.6753 L23: -2.5876
REMARK 3 S TENSOR
REMARK 3 S11: -0.1907 S12: 0.8825 S13: 0.2016
REMARK 3 S21: -0.9691 S22: 0.7516 S23: 0.8474
REMARK 3 S31: 0.6852 S32: -0.9941 S33: -0.3334
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 0 THROUGH 59 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.4887 71.3558 51.6476
REMARK 3 T TENSOR
REMARK 3 T11: 0.3502 T22: 0.6691
REMARK 3 T33: 0.6592 T12: 0.0076
REMARK 3 T13: 0.0369 T23: 0.3827
REMARK 3 L TENSOR
REMARK 3 L11: 2.6047 L22: 5.3926
REMARK 3 L33: 6.2173 L12: -3.0643
REMARK 3 L13: 4.0220 L23: -4.8272
REMARK 3 S TENSOR
REMARK 3 S11: 0.1008 S12: 0.4221 S13: 0.5575
REMARK 3 S21: -0.1856 S22: 0.2707 S23: 0.5264
REMARK 3 S31: 0.2840 S32: -0.6441 S33: -0.3703
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 60 THROUGH 124 )
REMARK 3 ORIGIN FOR THE GROUP (A): 58.3744 54.7479 72.2231
REMARK 3 T TENSOR
REMARK 3 T11: 0.3910 T22: 0.1848
REMARK 3 T33: 0.2298 T12: 0.0749
REMARK 3 T13: 0.1429 T23: 0.0362
REMARK 3 L TENSOR
REMARK 3 L11: 8.3267 L22: 3.2517
REMARK 3 L33: 4.8428 L12: -2.5230
REMARK 3 L13: 3.2299 L23: -1.1942
REMARK 3 S TENSOR
REMARK 3 S11: 0.1558 S12: -0.1137 S13: -0.0156
REMARK 3 S21: 0.1977 S22: 0.0326 S23: -0.0800
REMARK 3 S31: 0.6946 S32: 0.3835 S33: -0.1521
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5I0Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-FEB-16.
REMARK 100 THE DEPOSITION ID IS D_1000218008.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-APR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47421
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.290
REMARK 200 RESOLUTION RANGE LOW (A) : 49.533
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 40.50
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 46.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.29
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 32.60
REMARK 200 R MERGE FOR SHELL (I) : 1.00000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.220
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHENIX 1.9_1692
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 76.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M AMMONIUM SULFATE, 0.1 M BIS-TRIS
REMARK 280 PROPANE PH 7.0, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
REMARK 290 13555 Y+1/4,X+3/4,-Z+3/4
REMARK 290 14555 -Y+1/4,-X+1/4,-Z+1/4
REMARK 290 15555 Y+3/4,-X+3/4,Z+1/4
REMARK 290 16555 -Y+3/4,X+1/4,Z+3/4
REMARK 290 17555 X+1/4,Z+3/4,-Y+3/4
REMARK 290 18555 -X+3/4,Z+1/4,Y+3/4
REMARK 290 19555 -X+1/4,-Z+1/4,-Y+1/4
REMARK 290 20555 X+3/4,-Z+3/4,Y+1/4
REMARK 290 21555 Z+1/4,Y+3/4,-X+3/4
REMARK 290 22555 Z+3/4,-Y+3/4,X+1/4
REMARK 290 23555 -Z+3/4,Y+1/4,X+3/4
REMARK 290 24555 -Z+1/4,-Y+1/4,-X+1/4
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 74.29900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 74.29900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 74.29900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 74.29900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 74.29900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 74.29900
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 74.29900
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 74.29900
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 74.29900
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 74.29900
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 74.29900
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 74.29900
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 74.29900
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 74.29900
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 74.29900
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 74.29900
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 74.29900
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 74.29900
REMARK 290 SMTRY1 13 0.000000 1.000000 0.000000 37.14950
REMARK 290 SMTRY2 13 1.000000 0.000000 0.000000 111.44850
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 111.44850
REMARK 290 SMTRY1 14 0.000000 -1.000000 0.000000 37.14950
REMARK 290 SMTRY2 14 -1.000000 0.000000 0.000000 37.14950
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 37.14950
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 111.44850
REMARK 290 SMTRY2 15 -1.000000 0.000000 0.000000 111.44850
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 37.14950
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 111.44850
REMARK 290 SMTRY2 16 1.000000 0.000000 0.000000 37.14950
REMARK 290 SMTRY3 16 0.000000 0.000000 1.000000 111.44850
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 37.14950
REMARK 290 SMTRY2 17 0.000000 0.000000 1.000000 111.44850
REMARK 290 SMTRY3 17 0.000000 -1.000000 0.000000 111.44850
REMARK 290 SMTRY1 18 -1.000000 0.000000 0.000000 111.44850
REMARK 290 SMTRY2 18 0.000000 0.000000 1.000000 37.14950
REMARK 290 SMTRY3 18 0.000000 1.000000 0.000000 111.44850
REMARK 290 SMTRY1 19 -1.000000 0.000000 0.000000 37.14950
REMARK 290 SMTRY2 19 0.000000 0.000000 -1.000000 37.14950
REMARK 290 SMTRY3 19 0.000000 -1.000000 0.000000 37.14950
REMARK 290 SMTRY1 20 1.000000 0.000000 0.000000 111.44850
REMARK 290 SMTRY2 20 0.000000 0.000000 -1.000000 111.44850
REMARK 290 SMTRY3 20 0.000000 1.000000 0.000000 37.14950
REMARK 290 SMTRY1 21 0.000000 0.000000 1.000000 37.14950
REMARK 290 SMTRY2 21 0.000000 1.000000 0.000000 111.44850
REMARK 290 SMTRY3 21 -1.000000 0.000000 0.000000 111.44850
REMARK 290 SMTRY1 22 0.000000 0.000000 1.000000 111.44850
REMARK 290 SMTRY2 22 0.000000 -1.000000 0.000000 111.44850
REMARK 290 SMTRY3 22 1.000000 0.000000 0.000000 37.14950
REMARK 290 SMTRY1 23 0.000000 0.000000 -1.000000 111.44850
REMARK 290 SMTRY2 23 0.000000 1.000000 0.000000 37.14950
REMARK 290 SMTRY3 23 1.000000 0.000000 0.000000 111.44850
REMARK 290 SMTRY1 24 0.000000 0.000000 -1.000000 37.14950
REMARK 290 SMTRY2 24 0.000000 -1.000000 0.000000 37.14950
REMARK 290 SMTRY3 24 -1.000000 0.000000 0.000000 37.14950
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 0.000000 0.000000 1.000000 -37.14950
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 111.44850
REMARK 350 BIOMT3 2 1.000000 0.000000 0.000000 37.14950
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 289 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 302 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 38
REMARK 465 PRO A 39
REMARK 465 GLY A 40
REMARK 465 SER A 41
REMARK 465 ASN A 42
REMARK 465 SER A 43
REMARK 465 LYS A 44
REMARK 465 ASN A 45
REMARK 465 PRO A 46
REMARK 465 VAL A 47
REMARK 465 PRO A 48
REMARK 465 VAL A 49
REMARK 465 LYS A 50
REMARK 465 LYS A 51
REMARK 465 GLU A 52
REMARK 465 LYS A 87
REMARK 465 VAL A 88
REMARK 465 GLU A 89
REMARK 465 GLU A 90
REMARK 465 GLU A 91
REMARK 465 HIS A 92
REMARK 465 LYS A 93
REMARK 465 LYS A 94
REMARK 465 ASP A 95
REMARK 465 HIS A 96
REMARK 465 GLU A 97
REMARK 465 LYS A 98
REMARK 465 LEU A 99
REMARK 465 GLU A 100
REMARK 465 LYS A 101
REMARK 465 LYS A 102
REMARK 465 SER A 103
REMARK 465 GLU A 104
REMARK 465 ASP A 105
REMARK 465 VAL A 106
REMARK 465 GLU A 107
REMARK 465 ARG A 108
REMARK 465 HIS A 109
REMARK 465 TYR A 110
REMARK 465 LEU A 111
REMARK 465 ARG A 112
REMARK 465 GLN A 113
REMARK 465 LEU A 114
REMARK 465 ASP A 115
REMARK 465 GLN A 116
REMARK 465 GLU A 117
REMARK 465 TYR A 118
REMARK 465 LYS A 119
REMARK 465 GLU A 120
REMARK 465 GLN A 121
REMARK 465 GLN A 122
REMARK 465 GLU A 123
REMARK 465 ARG A 124
REMARK 465 GLN A 125
REMARK 465 LYS A 126
REMARK 465 ASN A 127
REMARK 465 LEU A 128
REMARK 465 GLU A 129
REMARK 465 GLU A 130
REMARK 465 LEU A 131
REMARK 465 GLU A 132
REMARK 465 ARG A 133
REMARK 465 GLN A 134
REMARK 465 SER A 135
REMARK 465 GLN A 136
REMARK 465 ARG A 137
REMARK 465 GLU A 138
REMARK 465 VAL A 139
REMARK 465 GLU A 140
REMARK 465 LYS A 141
REMARK 465 GLY B -3
REMARK 465 PRO B -2
REMARK 465 GLY B -1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NH1 ARG B 66 O HOH B 201 2.04
REMARK 500 O HOH B 269 O HOH B 305 2.08
REMARK 500 O ARG B 64 O HOH B 201 2.12
REMARK 500 NE ARG B 66 O HOH B 202 2.18
REMARK 500 O HOH B 215 O HOH B 218 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 208 O HOH B 300 21545 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 57 24.98 -79.22
REMARK 500 ALA A 58 10.33 90.23
REMARK 500 ILE B 16 50.03 35.69
REMARK 500 THR B 21 0.21 -54.72
REMARK 500 GLN B 44 53.06 -100.93
REMARK 500 THR B 80 -73.52 -129.95
REMARK 500 PHE B 84 123.94 -38.43
REMARK 500 ASP B 110 -123.21 57.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU A 59 LEU A 60 139.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5HYU RELATED DB: PDB
REMARK 900 RELATED ID: 5HYP RELATED DB: PDB
REMARK 900 RELATED ID: 5HYT RELATED DB: PDB
REMARK 900 RELATED ID: 5HZP RELATED DB: PDB
DBREF 5I0Q A 42 141 UNP P50468 M21_STRPY 42 141
DBREF 5I0Q B 1 124 UNP P04003 C4BPA_HUMAN 49 172
SEQADV 5I0Q GLY A 38 UNP P50468 EXPRESSION TAG
SEQADV 5I0Q PRO A 39 UNP P50468 EXPRESSION TAG
SEQADV 5I0Q GLY A 40 UNP P50468 EXPRESSION TAG
SEQADV 5I0Q SER A 41 UNP P50468 EXPRESSION TAG
SEQADV 5I0Q ALA A 65 UNP P50468 LYS 65 ENGINEERED MUTATION
SEQADV 5I0Q ALA A 66 UNP P50468 ASN 66 ENGINEERED MUTATION
SEQADV 5I0Q GLY B -3 UNP P04003 EXPRESSION TAG
SEQADV 5I0Q PRO B -2 UNP P04003 EXPRESSION TAG
SEQADV 5I0Q GLY B -1 UNP P04003 EXPRESSION TAG
SEQADV 5I0Q SER B 0 UNP P04003 EXPRESSION TAG
SEQRES 1 A 104 GLY PRO GLY SER ASN SER LYS ASN PRO VAL PRO VAL LYS
SEQRES 2 A 104 LYS GLU ALA LYS LEU SER GLU ALA GLU LEU HIS ASP LYS
SEQRES 3 A 104 ILE ALA ALA LEU GLU GLU GLU LYS ALA GLU LEU PHE GLU
SEQRES 4 A 104 LYS LEU ASP LYS VAL GLU GLU GLU HIS LYS LYS VAL GLU
SEQRES 5 A 104 GLU GLU HIS LYS LYS ASP HIS GLU LYS LEU GLU LYS LYS
SEQRES 6 A 104 SER GLU ASP VAL GLU ARG HIS TYR LEU ARG GLN LEU ASP
SEQRES 7 A 104 GLN GLU TYR LYS GLU GLN GLN GLU ARG GLN LYS ASN LEU
SEQRES 8 A 104 GLU GLU LEU GLU ARG GLN SER GLN ARG GLU VAL GLU LYS
SEQRES 1 B 128 GLY PRO GLY SER ASN CYS GLY PRO PRO PRO THR LEU SER
SEQRES 2 B 128 PHE ALA ALA PRO MET ASP ILE THR LEU THR GLU THR ARG
SEQRES 3 B 128 PHE LYS THR GLY THR THR LEU LYS TYR THR CYS LEU PRO
SEQRES 4 B 128 GLY TYR VAL ARG SER HIS SER THR GLN THR LEU THR CYS
SEQRES 5 B 128 ASN SER ASP GLY GLU TRP VAL TYR ASN THR PHE CYS ILE
SEQRES 6 B 128 TYR LYS ARG CYS ARG HIS PRO GLY GLU LEU ARG ASN GLY
SEQRES 7 B 128 GLN VAL GLU ILE LYS THR ASP LEU SER PHE GLY SER GLN
SEQRES 8 B 128 ILE GLU PHE SER CYS SER GLU GLY PHE PHE LEU ILE GLY
SEQRES 9 B 128 SER THR THR SER ARG CYS GLU VAL GLN ASP ARG GLY VAL
SEQRES 10 B 128 GLY TRP SER HIS PRO LEU PRO GLN CYS GLU ILE
FORMUL 3 HOH *132(H2 O)
HELIX 1 AA1 GLU A 59 HIS A 85 1 27
SHEET 1 AA1 4 ALA B 11 PRO B 13 0
SHEET 2 AA1 4 THR B 28 CYS B 33 -1 O THR B 32 N ALA B 12
SHEET 3 AA1 4 THR B 45 CYS B 48 -1 O LEU B 46 N LEU B 29
SHEET 4 AA1 4 TRP B 54 VAL B 55 -1 O VAL B 55 N THR B 47
SHEET 1 AA2 2 TYR B 37 ARG B 39 0
SHEET 2 AA2 2 CYS B 60 TYR B 62 -1 O ILE B 61 N VAL B 38
SHEET 1 AA3 4 GLY B 74 ILE B 78 0
SHEET 2 AA3 4 GLN B 87 CYS B 92 -1 O GLU B 89 N GLU B 77
SHEET 3 AA3 4 THR B 103 GLN B 109 -1 O SER B 104 N ILE B 88
SHEET 4 AA3 4 GLY B 112 TRP B 115 -1 O GLY B 114 N GLU B 107
SHEET 1 AA4 2 PHE B 97 ILE B 99 0
SHEET 2 AA4 2 GLN B 121 GLU B 123 -1 O GLU B 123 N PHE B 97
SSBOND 1 CYS B 2 CYS B 48 1555 1555 2.06
SSBOND 2 CYS B 33 CYS B 60 1555 1555 2.05
SSBOND 3 CYS B 65 CYS B 106 1555 1555 2.10
SSBOND 4 CYS B 92 CYS B 122 1555 1555 2.04
CRYST1 148.598 148.598 148.598 90.00 90.00 90.00 P 43 3 2 24
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.006730 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006730 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006730 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
